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Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra.

A luciferin-binding protein ( LBP), which binds and protects from autoxidation the substrate of the circadian bioluminescent reaction of Gonyaulax polyedra, has been purified to near homogeneity. The purified protein is a dimer with two identical 72-kDa subunits, and an isoelectric point of 6. 7. LBP is a major component of the cells, comprising about 1% of the total protein during the night phase, but drops to only about 0.1% during the day. The luciferin is protected from autoxidation by binding to LBP, and one luciferin is bound per dimer at alkaline pH (Ka approximately 5 x 10(7) M-1). The protein undergoes a conformational change with release of luciferin at pH values below 7, concurrent with an activation of Gonyaulax luciferase. LBP thus has a dual role in the circadian bioluminescent system.[1]

References

  1. Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra. Morse, D., Pappenheimer, A.M., Hastings, J.W. J. Biol. Chem. (1989) [Pubmed]
 
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